NAGH_CLOPE
ID NAGH_CLOPE Reviewed; 1628 AA.
AC P26831;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Hyaluronoglucosaminidase;
DE Short=Hyaluronidase;
DE EC=3.2.1.35;
DE AltName: Full=Mu toxin;
DE Flags: Precursor;
GN Name=nagH; OrderedLocusNames=CPE0191;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CPN50;
RX PubMed=8177218; DOI=10.1007/bf00280319;
RA Canard B., Garnier T., Saint-Joanis B., Cole S.T.;
RT "Molecular genetic analysis of the nagH gene encoding a hyaluronidase of
RT Clostridium perfringens.";
RL Mol. Gen. Genet. 243:215-224(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Putative virulence factor which is likely to act on
CC connective tissue during gas gangrene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- INTERACTION:
CC P26831; Q8XL08: nagJ; NbExp=3; IntAct=EBI-15722600, EBI-15722628;
CC P26831; Q8XMY5: nanJ; NbExp=2; IntAct=EBI-15722600, EBI-15722735;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- CAUTION: The partially purified protein from strain CPN50 is
CC approximately 70 kDa smaller than the sequence indicated here.
CC {ECO:0000305}.
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DR EMBL; M81878; AAA23259.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79897.1; -; Genomic_DNA.
DR PIR; S43904; S43904.
DR RefSeq; WP_011009663.1; NC_003366.1.
DR PDB; 2JNK; NMR; -; A=1498-1628.
DR PDB; 2OZN; X-ray; 1.60 A; B=1498-1628.
DR PDB; 2W1Q; X-ray; 1.60 A; A/B=807-975.
DR PDB; 2W1S; X-ray; 1.45 A; A/B=807-975.
DR PDB; 2W1U; X-ray; 2.00 A; A/B/C/D=807-975.
DR PDB; 2WDB; X-ray; 2.03 A; A/B/C/D=807-975.
DR PDBsum; 2JNK; -.
DR PDBsum; 2OZN; -.
DR PDBsum; 2W1Q; -.
DR PDBsum; 2W1S; -.
DR PDBsum; 2W1U; -.
DR PDBsum; 2WDB; -.
DR AlphaFoldDB; P26831; -.
DR BMRB; P26831; -.
DR SMR; P26831; -.
DR DIP; DIP-46268N; -.
DR IntAct; P26831; 3.
DR STRING; 195102.gene:10489435; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR PRIDE; P26831; -.
DR EnsemblBacteria; BAB79897; BAB79897; BAB79897.
DR KEGG; cpe:CPE0191; -.
DR HOGENOM; CLU_001501_1_1_9; -.
DR OMA; HTEYAEV; -.
DR BRENDA; 4.2.2.1; 1503.
DR EvolutionaryTrace; P26831; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SMART; SM00231; FA58C; 1.
DR SUPFAM; SSF49785; SSF49785; 4.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Toxin; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1628
FT /note="Hyaluronoglucosaminidase"
FT /id="PRO_0000021787"
FT DOMAIN 781..953
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1573..1628
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT VARIANT 147
FT /note="G -> A (in strain: CPN50)"
FT VARIANT 172..175
FT /note="KIQS -> EIKN (in strain: CPN50)"
FT VARIANT 250
FT /note="V -> M (in strain: CPN50)"
FT VARIANT 548
FT /note="A -> E (in strain: CPN50)"
FT VARIANT 558
FT /note="D -> E (in strain: CPN50)"
FT VARIANT 614
FT /note="G -> S (in strain: CPN50)"
FT VARIANT 944
FT /note="I -> V (in strain: CPN50)"
FT VARIANT 950
FT /note="N -> S (in strain: CPN50)"
FT VARIANT 979
FT /note="T -> I (in strain: CPN50)"
FT VARIANT 982
FT /note="I -> L (in strain: CPN50)"
FT VARIANT 1042
FT /note="I -> F (in strain: CPN50)"
FT VARIANT 1043..1628
FT /note="Missing (in strain: CPN50)"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 817..821
FT /evidence="ECO:0007829|PDB:2W1S"
FT HELIX 823..826
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 835..838
FT /evidence="ECO:0007829|PDB:2W1S"
FT HELIX 840..843
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 850..868
FT /evidence="ECO:0007829|PDB:2W1S"
FT TURN 873..876
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 880..892
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 894..900
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 909..928
FT /evidence="ECO:0007829|PDB:2W1S"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:2W1U"
FT STRAND 936..944
FT /evidence="ECO:0007829|PDB:2W1S"
FT TURN 946..948
FT /evidence="ECO:0007829|PDB:2W1U"
FT HELIX 1500..1515
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 1518..1521
FT /evidence="ECO:0007829|PDB:2OZN"
FT HELIX 1529..1544
FT /evidence="ECO:0007829|PDB:2OZN"
FT HELIX 1551..1570
FT /evidence="ECO:0007829|PDB:2OZN"
FT TURN 1575..1578
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 1583..1585
FT /evidence="ECO:0007829|PDB:2OZN"
FT HELIX 1588..1596
FT /evidence="ECO:0007829|PDB:2OZN"
FT TURN 1597..1599
FT /evidence="ECO:0007829|PDB:2OZN"
FT TURN 1604..1606
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 1611..1613
FT /evidence="ECO:0007829|PDB:2OZN"
FT HELIX 1616..1627
FT /evidence="ECO:0007829|PDB:2OZN"
SQ SEQUENCE 1628 AA; 182475 MW; D4252A2512BBED69 CRC64;
MNKNIRKIIT STVLAAMTIS VLPSNLVVFA TDGITENFYE IYPKPQEISY SGGEFQISDE
INIVYDDGID TYTKKRVDEV LEASNLEATV SNEIVPGKTN FLVGINESGG VVDNYFNKNI
PHDESFFDEK MDANIVSVKD GVIGVIGEDT DSAFYGVTTL KHVFNQLEEG NKIQSFRADD
YAEVAHRGFI EGYYGNPWSN EDRAELMKFG GDYKLNQYVF APKDDPYHNS KWRDLYPEEK
LSEIKKLAQV GNETKNRYVY ALHPFMNNPV RFDTEENYQN DLGVIKAKFT QLLENDVRQF
AILADDASAP AQGASMYVKL LTDLTRWLEE QQSTYPDLKT DLMFCPSDYY GNGSSAQLKE
LNKAEDNVSI VMTGGRIWGE VDENFANNFM NNISTEGHPG RAPFFWINWP CSDNSKQHLI
MGGNDTFLHP GVDPSKIDGI VLNPMQQAEA NKSALFAIAD YAWNIWDNKE EADENWNDSF
KYMDHGTAEE TNSSLALREI SKHMINQNMD GRVRPLQESV ELAPKLEAFK QKYDSGASIK
EDALELIAEF TNLQKAADYY KNNPGNERTR DQIIYWLNCW EDTMDAAIGY LKSAIAIEEG
DDEAAWANYS EAQGAFEKSK TYGFHYVDHT EYAEVGVQHI VPFIKSMGQN LSVVIGSIVD
PNRIIATYIS NRQDAPTGNP DNIFDNNAST ELVYKNPNRI DVGTYVGVKY SNPITLNNVE
FLMGANSNPN DTMQKAKIQY TVDGREWIDL EEGVEYTMPG AIKVENLDLK VRGVRLIATE
ARENTWLGVR DINVNKKEDS NSGVEFNPSL IRSESWQVYE GNEANLLDGD DNTGVWYKTL
NGDTSLAGEF IGLDLGKEIK LDGIRFVIGK NGGGSSDKWN KFKLEYSLDN ESWTTIKEYD
KTGAPAGKDV IEESFETPIS AKYIRLTNME NINKWLTFSE FAIISDELEN AGNKENVYTN
TELDLLSLAK EDVTKLIPTD DISLNHGEYI GVKLNRIKDL SNINLEISND TGLKLQSSMN
GVEWTEITDK NTLEDGRYVR LINTSNEAVN FNLTKFEVNS NEVYEPSLVD AYVGDDGAKK
AVDGDLKTRV KFLGAPSTGD TIVYDLGQEI LVDNLKYVVL DTEVDHVRDG KIQLSLDGET
WTDAITIGDG VENGVDDMFS TPLKNGYKHG NQSGGIVPID SAYVEGDNLN QKARYVRILF
TAPYRHRWTV INELMINNGE YISTVNDPTY ISNPIEERGF APSNLRDGNL TTSYKPNTNN
GEISEGSITY RLSEKTDVRK VTIVQSGSSI SNAKVMARVG DGSENVTDQW VQLGTLSNSL
NEFINRDYNN IYEIKIEWTD VAPNIYEIIT LNQEFEFPVN DSLKAKYDEL INLSGDEYTL
SSFETLKEAL NEAKSILDDS NSSQKKIDKA LEKLNKAEER LDLRATDFED FNKVLTLGNS
LVEEEYTAES WALFSEVLEA ANEANKNKAD YTQDQINQIV IDLDASIKAL VKETPEVDKT
NLGELINQGK SLLDESVEGF NVGEYHKGAK DGLTVEINKA EEVFNKEDAT EEEINLAKES
LEGAIARFNS LLIEESTGDF NGNGKIDIGD LAMVSKNIGS TTNTSLDLNK DGSIDEYEIS
FINHRILN
